C1139_DROME
ID C1139_DROME Reviewed; 451 AA.
AC Q9W056;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Proton-coupled amino acid transporter-like protein CG1139 {ECO:0000305};
GN ORFNames=CG1139 {ECO:0000312|FlyBase:FBgn0035300};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM50914.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50914.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15843412; DOI=10.1242/dev.01821;
RA Goberdhan D.C., Meredith D., Boyd C.A., Wilson C.;
RT "PAT-related amino acid transporters regulate growth via a novel mechanism
RT that does not require bulk transport of amino acids.";
RL Development 132:2365-2375(2005).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=22574197; DOI=10.1371/journal.pone.0036616;
RA Oegmundsdottir M.H., Heublein S., Kazi S., Reynolds B., Visvalingam S.M.,
RA Shaw M.K., Goberdhan D.C.;
RT "Proton-assisted amino acid transporter PAT1 complexes with Rag GTPases and
RT activates TORC1 on late endosomal and lysosomal membranes.";
RL PLoS ONE 7:E36616-E36616(2012).
CC -!- FUNCTION: Amino acid transporter which has pH-dependent electrogenic
CC transport activity for alanine, glycine and proline (PubMed:15843412).
CC Plays a role in positive regulation of growth by directly or indirectly
CC modulating the effects of the TOR signaling pathway (PubMed:15843412,
CC PubMed:22574197). {ECO:0000269|PubMed:15843412,
CC ECO:0000269|PubMed:22574197}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAF47603.1; -; Genomic_DNA.
DR EMBL; AY119054; AAM50914.1; -; mRNA.
DR RefSeq; NP_647686.1; NM_139429.2.
DR AlphaFoldDB; Q9W056; -.
DR SMR; Q9W056; -.
DR IntAct; Q9W056; 2.
DR STRING; 7227.FBpp0072724; -.
DR GlyGen; Q9W056; 2 sites.
DR PaxDb; Q9W056; -.
DR PRIDE; Q9W056; -.
DR DNASU; 38264; -.
DR EnsemblMetazoa; FBtr0072845; FBpp0072724; FBgn0035300.
DR GeneID; 38264; -.
DR KEGG; dme:Dmel_CG1139; -.
DR UCSC; CG1139-RA; d. melanogaster.
DR FlyBase; FBgn0035300; CG1139.
DR VEuPathDB; VectorBase:FBgn0035300; -.
DR eggNOG; KOG1304; Eukaryota.
DR GeneTree; ENSGT00940000167965; -.
DR HOGENOM; CLU_009646_0_1_1; -.
DR InParanoid; Q9W056; -.
DR OMA; VYQLGIC; -.
DR OrthoDB; 464614at2759; -.
DR PhylomeDB; Q9W056; -.
DR Reactome; R-DME-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-DME-428559; Proton-coupled neutral amino acid transporters.
DR Reactome; R-DME-71240; Tryptophan catabolism.
DR BioGRID-ORCS; 38264; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38264; -.
DR PRO; PR:Q9W056; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035300; Expressed in adult Malpighian tubule (Drosophila) and 12 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003333; P:amino acid transmembrane transport; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Growth regulation;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..451
FT /note="Proton-coupled amino acid transporter-like protein
FT CG1139"
FT /id="PRO_0000436783"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..80
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..167
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..237
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..320
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..382
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..451
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 451 AA; 50042 MW; 116947A3BC566609 CRC64;
MNDDIKTVTV YPTTLELTTP TKSANGSNDD YDPHQHRELK NPTTNFQTFA HFLKASVGTG
VLAMPSAFAH AGYVNGTLLT LIIGSLALYC LHILIKCMYI LCKRQRVPYV SFSQAMNLGL
KQGPPWLRCL APIAVPFVDG FLAFYHFGIC CVYVVFIAES IKQLVDEYLV VWDVRIHMCI
IIVPLLLIYS IKNLKLLAPF SSAANLLLLV GFGIILYYIF EELPPLSERD PFVAAGKLPT
FFGTVLFALE AVGVILAIEE NMATPKSFVG PCGILNSGMS IVLGLYVLLG FFGYWKYGNE
SEGSITLNIP QSEIPAQVVK VFFAITTWIS YALQGYVTAH ILWDKYLAKR FKETRQTFYE
LIFRAIIVLL TFGCAVAIPD LSVFLSLVGS FCLSILGLIF PVLLQICVQY TEGYGPFRIK
LIINLLLLCF GIFGGVVGTY VSILDIIAVY K
